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Catalysts
Special Issues
Biocatalytic Polymer Synthesis
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Biocatalytic Polymer Synthesis

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (28 February 2019) | Viewed by 11172

Special Issue Editors

Dr. Ren Wei

E-Mail Website
Guest Editor
Univ Leipzig, Dept Microbiol & Bioproc Technol, Inst Biochem, Johannisallee 21-23, D-04103 Leipzig, Germany
Interests: enzymatic polymer degradation; enzymatic polyester synthesis; microbial biotechnology; protein engineering; metagenomics
Special Issues, Collections and Topics in MDPI journals
Dr. Ren Wei

E-Mail Website
Guest Editor
Junior Research Group Plastic Biodegradation, Department of Biotechnology and Enzyme Catalysis, Institute for Biochemistry, University of Greifswald, Greifswald, Germany
Interests: microbial biotechnology; biocatalysis; protein engineering; plastic degradation; plastic recycling
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In recent years, bio-derived polymers have become of increasing interest; they have the potential to replace petroleum-based counterparts, which are regarded as much less eco-friendly. In this context, those polymers that have been derived not only from biological raw materials but also using biocatalytic approaches are even more compelling due to the ‘green’ advantages of synthetic methods including clean processes, low energy consumption, mild reaction conditions, and the biodegradable nature of product polymers, etc. Various enzyme classes have proven to catalyze the synthesis of a wide range of functional polymers both in vivo and in vitro. Depending on the applied biocatalysts, beneficial features of the enzymatic synthesis in living cells, e.g. superior catalytic efficiency and high enantio-, regio-, and chemoselectivity, can also be achieved in vitro. Hence, selected enzymes have emerged as powerful and versatile catalysts, promising the synthesis of novel macromolecules, especially those that are hardly accessed by conventional chemical methodologies.

This Special Issue welcomes scientific contributions covering the recent progress and advances in the field of "Biocatalytic Polymer Synthesis". This includes, but is not restricted to, the design and engineering of novel biocatalysts, their applications in the synthesis of various polymers and specified monomers, innovative enzyme immobilization technologies, in vivo polymer modifications, and polymerizations highlighting involved biocatalysts.

Dr. Ren Wei
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Bio-derived Polymers
  • Biocatalytic polycondensation
  • Enzymatic polyester synthesis
  • Enzyme immobilization
  • Polymerization using whole-cell catalysts

Published Papers (3 papers)

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9 pages, 3739 KiB  
Article
Preparation of Amylose-Carboxymethyl Cellulose Conjugated Supramolecular Networks by Phosphorylase-Catalyzed Enzymatic Polymerization
by Jun-ichi Kadokawa, Takuya Shoji and Kazuya Yamamoto
Catalysts 2019, 9(3), 211; https://doi.org/10.3390/catal9030211 - 26 Feb 2019
Cited by 6 | Viewed by 2952
Abstract
Enzymatic polymerization has been noted as a powerful method to precisely synthesize polymers with complicated structures, such as polysaccharides, which are not commonly prepared by conventional polymerization. Phosphorylase is one of the enzymes which have been used to practically synthesize well-defined polysaccharides. The [...] Read more.
Enzymatic polymerization has been noted as a powerful method to precisely synthesize polymers with complicated structures, such as polysaccharides, which are not commonly prepared by conventional polymerization. Phosphorylase is one of the enzymes which have been used to practically synthesize well-defined polysaccharides. The phosphorylase-catalyzed enzymatic polymerization is conducted using α-d-glucose 1-phosphate as a monomer, and maltooligosaccharide as a primer, respectively, to obtain amylose. Amylose is known to form supramolecules owing to its helical conformation, that is, inclusion complex and double helix, in which the formation is depended on whether a guest molecule is present or not. In this paper, we would like to report the preparation of amylose-carboxymethyl cellulose (CMC) conjugated supramolecular networks, by the phosphorylase-catalyzed enzymatic polymerization, using maltoheptaose primer-grafted CMC. When the enzymatic polymerization was carried out using the graft copolymer, either in the presence or in the absence of a guest polymer poly (ε-caprolactone) (PCL), the enzymatically elongated amylose chains from the primers on the CMC main-chain formed double helixes or inclusion complexes, depending on the amounts of PCL, which acted as cross-linking points for the construction of network structures. Accordingly, the reaction mixtures totally turned into hydrogels, regardless of the structures of supramolecular cross-linking points. Full article
(This article belongs to the Special Issue Biocatalytic Polymer Synthesis)
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10 pages, 2287 KiB  
Article
A Novel High-Throughput Assay Enables the Direct Identification of Acyltransferases
by Lukas Reisky, Vishnu S. T. Srinivasamurthy, Chris P. S. Badenhorst, Simon P. Godehard and Uwe T. Bornscheuer
Catalysts 2019, 9(1), 64; https://doi.org/10.3390/catal9010064 - 09 Jan 2019
Cited by 13 | Viewed by 3739
Abstract
Acyltransferases are enzymes that are capable of catalyzing the transesterification of non-activated esters in an aqueous environment and therefore represent interesting catalysts for applications in various fields. However, only a few acyltransferases have been identified so far, which can be explained by the [...] Read more.
Acyltransferases are enzymes that are capable of catalyzing the transesterification of non-activated esters in an aqueous environment and therefore represent interesting catalysts for applications in various fields. However, only a few acyltransferases have been identified so far, which can be explained by the lack of a simple, broadly applicable high-throughput assay for the identification of these enzymes from large libraries. Here, we present the development of such an assay that is based on the enzymatic formation of oligocarbonates from dimethyl carbonate and 1,6-hexanediol. In contrast to the monomers used as substrates, the oligomers are not soluble in the aqueous environment and form a precipitate which is used to detect enzyme activity by the naked eye, by absorbance or by fluorescence measurements. With activity detected and thus confirmed for the enzymes Est8 and MsAcT, the assay enabled the first identification of acyltransferases that act on carbonates. It will thus allow for the discovery of further efficient acyltransferases or of more efficient variants via enzyme engineering. Full article
(This article belongs to the Special Issue Biocatalytic Polymer Synthesis)
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12 pages, 1364 KiB  
Article
Efficient Physisorption of Candida Antarctica Lipase B on Polypropylene Beads and Application for Polyester Synthesis
by Simone Weinberger, Alessandro Pellis, James W. Comerford, Thomas J. Farmer and Georg M. Guebitz
Catalysts 2018, 8(9), 369; https://doi.org/10.3390/catal8090369 - 31 Aug 2018
Cited by 19 | Viewed by 4115
Abstract
In the present work, Candida antarctica lipase B (CaLB) was adsorbed onto polypropylene beads using different reaction conditions, in order to investigate their influence on the immobilization process and the enzyme activity of the preparations in polymerization reactions. In general, lower salt concentrations [...] Read more.
In the present work, Candida antarctica lipase B (CaLB) was adsorbed onto polypropylene beads using different reaction conditions, in order to investigate their influence on the immobilization process and the enzyme activity of the preparations in polymerization reactions. In general, lower salt concentrations were more favorable for the binding of enzyme to the carrier. Polymerisation of dimethyl adipate (DMA) and 1,4-butanediol (BDO) was investigated in thin-film systems at 70 °C and at both atmosphere pressure (1000 mbar) and 70 mbar. Conversion rates and molecular masses of the reaction products were compared with reactions catalyzed by CaLB in its commercially available form, known as Novozym 435 (CaLB immobilized on macroporous acrylic resin). The best results according to molecular weight and monomer conversion after 24 h reaction time were obtained with CaLB immobilized in 0.1 M Na2HPO4\NaH2PO4 buffer at pH 8, producing polyesters with 4 kDa at conversion rates of 96% under low pressure conditions. The stability of this preparation was studied in a simulated continuous polymerization process at 70 °C, 70 mbar for 4 h reaction time. The data of this continuous polymerizations show that the preparation produces lower molecular weights at lower conversion rates, but is comparable to the commercial enzyme concerning stability for 10 cycles. However, after 24 h reaction time, using our optimum preparation, higher molecular weight polyesters (4 kDa versus 3.1 kDa) were obtained when compared to Novozym 435. Full article
(This article belongs to the Special Issue Biocatalytic Polymer Synthesis)
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